Evidence map›Paper›PMID 26351290›Full record

ArticlePhysiological genomics2015

Global deletion of BCATm increases expression of skeletal muscle genes associated with protein turnover.

Christopher J Lynch, Scot R Kimball, Yuping Xu, Anna C Salzberg, Yuka Imamura Kawasawa

Abstract read
In one paragraph

Article in Physiological genomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 37% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 17 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Christopher J LynchDepartment of Cellular and Molecular Physiology, College of Medicine, Penn State University, Hershey, Pennsylvania; clynch@psu.edu.ORCID http://orcid.org/0000-0003-2453-5838
Scot R KimballDepartment of Cellular and Molecular Physiology, College of Medicine, Penn State University, Hershey, Pennsylvania;
Yuping XuDepartment of Cellular and Molecular Physiology, College of Medicine, Penn State University, Hershey, Pennsylvania;
Anna C SalzbergThe Institute for Personalized Medicine, College of Medicine, Penn State University, Hershey, Pennsylvania;
Yuka Imamura KawasawaThe Institute for Personalized Medicine, College of Medicine, Penn State University, Hershey, Pennsylvania; Department of Pharmacology, College of Medicine, Penn State University, Hershey, Pennsylvania; and Department of Biochemistry and Molecular Biology, College of Medicine, Penn State University, Hershey, Pennsylvania.
Penn State Milton S. Hershey Medical Center · USPennsylvania State University · US

Funding

Role of Leucine Metabolism in Leucine SignalingR01DK062880 · NIDDK · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI LYNCH, CHRISTOPHER JOHN · 2003 to 2010
$2.8M
Mechanisms of drug side effects related to obesity and diabetesR01DK084428 · NIDDK · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI LYNCH, CHRISTOPHER JOHN · 2010 to 2013
$1.3M
NIDDK NIH HHS DK-084428NIDDK NIH HHS R01 DK062880NIDDK NIH HHS R01 DK084428
6 · The paper itself

Abstract

Consumption of a protein-containing meal by a fasted animal promotes protein accretion in skeletal muscle, in part through leucine stimulation of protein synthesis and indirectly through repression of protein degradation mediated by its metabolite, α-ketoisocaproate. Mice lacking the mitochondrial branched-chain aminotransferase (BCATm/Bcat2), which interconverts leucine and α-ketoisocaproate, exhibit elevated protein turnover. Here, the transcriptomes of gastrocnemius muscle from BCATm knockout (KO) and wild-type mice were compared by next-generation RNA sequencing (RNA-Seq) to identify potential adaptations associated with their persistently altered nutrient signaling. Statistically significant changes in the abundance of 1,486/∼39,010 genes were identified. Bioinformatics analysis of the RNA-Seq data indicated that pathways involved in protein synthesis [eukaryotic initiation factor (eIF)-2, mammalian target of rapamycin, eIF4, and p70S6K pathways including 40S and 60S ribosomal proteins], protein breakdown (e.g., ubiquitin mediated), and muscle degeneration (apoptosis, atrophy, myopathy, and cell death) were upregulated. Also in agreement with our previous observations, the abundance of mRNAs associated with reduced body size, glycemia, plasma insulin, and lipid signaling pathways was altered in BCATm KO mice. Consistently, genes encoding anaerobic and/or oxidative metabolism of carbohydrate, fatty acids, and branched chain amino acids were modestly but systematically reduced. Although there was no indication that muscle fiber type was different between KO and wild-type mice, a difference in the abundance of mRNAs associated with a muscular dystrophy phenotype was observed, consistent with the published exercise intolerance of these mice. The results suggest transcriptional adaptations occur in BCATm KO mice that along with altered nutrient signaling may contribute to their previously reported protein turnover, metabolic and exercise phenotypes.

Indexed as

Gene DeletionAnimalsMaleMiceMice, Inbred C57BLMice, KnockoutMuscle ProteinsMuscle, SkeletalTransaminasesBcat1 protein, mouseMuscle ProteinsTransaminasesbranched-chain amino acidsdystrophyeukaryotic initiation factor-2glycolysisintegrin-linked kinaseleucinemTORmyopathyprotein degradationprotein synthesissignalingTCA cycleα-ketoisocaproate

Identifiers

PMID26351290
PMCPMC4629004
OpenAlexW1871705593

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.